Functional study of an unsaturated glucoronyl hydrolase (UGL) of Leucoagaricus gongylophorus, a symbiotic fungus of leaf-cutting ants

• Grant number: 17/16005-2
• Support Opportunities: Scholarships in Brazil - Scientific Initiation
• Start date until: September 01, 2017
• End date until: January 01, 2020
• Field of knowledge: Physical Sciences and Mathematics - Chemistry - Organic Chemistry
• Principal Investigator: João Batista Fernandes
• Grantee: Melissa Tomaz Soares
• Host Institution: Centro de Ciências Exatas e de Tecnologia (CCET). Universidade Federal de São Carlos (UFSCAR). São Carlos , SP, Brazil
• Associated research grant: 12/25299-6 - Integrated studies for leaf cutting control, AP.TEM
• Associated scholarship(s): 18/26632-7 - Expression of acetylcholinesterase from Atta sexdens on insect cells, BE.EP.IC

Abstract

The search for new methodologies for the control of leaf cutting ants has been object of study of the Natural Products Group of the Department of Chemistry of UFSCar, coordinated by Prof. Dr. João Batista Fernandes, in collaboration with researchers from the Center for the Study of Social Insects - CEIS - UNESP, campus of Rio Claro. One of the aspects of the study is to explore the symbiosis between ants and the fungus L. gongylophorus, searching for compounds that inhibit the growth of the fungus, with the consequent control of the ants. There are few studies on unsaturated glucuronyl hydrolases (UGLs) of bacteria and not one of UGL of fungus has been so far characterized biochemically. Thus, it is quite interesting to see if the gene found in the cDNA library of the fungus L. gongylophorus actually encodes the synthesis of a UGL and characterize the enzyme from a biochemical point of view. In order to reach this objective, the characterization of the potential UGL enzyme of the fungus L. gongylophorus, several steps are necessary and in this CI project we propose the beginning of this study, with the cloning of the DNA that codifies the synthesis of the protein in plasmid suitable for its expression in P. pastoris and its partial purification for later functional characterization. (AU)